1anv

ADENOVIRUS 5 DBP/URANYL FLUORIDE SOAK

spinqualitylabelsall models 1anv, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1anv is a 1 chain structure with sequence from Human adenovirus 5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: IUM, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DNB2_ADE05 Binds cooperatively single-stranded DNA in a sequence-independent manner. Involved in DNA-replication, regulation of mRNA formation, and host-range specificity. Zinc is required for DNA binding. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Soaking crystals of the C-terminal DNA-binding domain of the adenovirus single-stranded DNA-binding protein with a buffer containing K(3)UO(2)F(5) results in a 9% change of the crystallographic c axis without destruction of the crystals or appreciable loss of resolution. The crystals belong to space group P2(1)2(1)2(1) with a = 79.7, b = 75.6 and c = 60.6 A. The three-dimensional structure has been refined to 2.7 A with a crystallographic R factor of 0.206. Antiparallel chains of protein molecules running through the entire crystal are linked by uranyl ions. The relative orientation of protein monomers is flexible, even in the crystalline state, and allows changes in the packing of the protein chains. Conformational change of the adenovirus DNA-binding protein induced by soaking crystals with K3UO2F5 solutions.,Kanellopoulos PN, Tsernoglou D, van der Vliet PC, Tucker PA Acta Crystallogr D Biol Crystallogr. 1996 Sep 1;52(Pt 5):942-5. PMID:15299602 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Single-stranded DNA-binding protein 3D structures

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